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6ze2

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'''Unreleased structure'''
 
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The entry 6ze2 is ON HOLD
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==FAD-dependent oxidoreductase from Chaetomium thermophilum==
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<StructureSection load='6ze2' size='340' side='right'caption='[[6ze2]], [[Resolution|resolution]] 1.31&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6ze2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ZE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ZE2 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.31&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FDA:DIHYDROFLAVINE-ADENINE+DINUCLEOTIDE'>FDA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6ze2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ze2 OCA], [https://pdbe.org/6ze2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ze2 RCSB], [https://www.ebi.ac.uk/pdbsum/6ze2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ze2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/G0SAW6_CHATD G0SAW6_CHATD]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The FAD-dependent oxidoreductase from Chaetomium thermophilum (CtFDO) is a novel thermostable glycoprotein from the glucose-methanol-choline (GMC) oxidoreductase superfamily. However, CtFDO shows no activity toward the typical substrates of the family and high-throughput screening with around 1000 compounds did not yield any strongly reacting substrate. Therefore, protein crystallography, including crystallographic fragment screening, with 42 fragments and 37 other compounds was used to describe the ligand-binding sites of CtFDO and to characterize the nature of its substrate. The structure of CtFDO reveals an unusually wide-open solvent-accessible active-site pocket with a unique His-Ser amino-acid pair putatively involved in enzyme catalysis. A series of six crystal structures of CtFDO complexes revealed five different subsites for the binding of aryl moieties inside the active-site pocket and conformational flexibility of the interacting amino acids when adapting to a particular ligand. The protein is capable of binding complex polyaromatic substrates of molecular weight greater than 500 Da.
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Authors:
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Crystallographic fragment screening-based study of a novel FAD-dependent oxidoreductase from Chaetomium thermophilum.,Svecova L, Ostergaard LH, Skalova T, Schnorr KM, Koval' T, Kolenko P, Stransky J, Sedlak D, Duskova J, Trundova M, Hasek J, Dohnalek J Acta Crystallogr D Struct Biol. 2021 Jun 1;77(Pt 6):755-775. doi:, 10.1107/S2059798321003533. Epub 2021 May 14. PMID:34076590<ref>PMID:34076590</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6ze2" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Chaetomium thermophilum var. thermophilum DSM 1495]]
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[[Category: Large Structures]]
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[[Category: Dohnalek J]]
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[[Category: Kolenko P]]
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[[Category: Koval T]]
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[[Category: Oestergaard LH]]
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[[Category: Skalova T]]
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[[Category: Svecova L]]

Current revision

FAD-dependent oxidoreductase from Chaetomium thermophilum

PDB ID 6ze2

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